Journal
FEBS LETTERS
Volume 590, Issue 5, Pages 619-630Publisher
WILEY
DOI: 10.1002/1873-3468.12099
Keywords
amyloid fibrils; electron microscopy; functional amyloid; homology modeling; peptide-analogs; zona pellucida
Funding
- European Community's Seventh Framework Programme (FP7) under BioStruct-X [283570]
- University of Athens
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Human zona pellucida (ZP) is composed of four glycoproteins, namely ZP1, ZP2, ZP3 and ZP4. ZP proteins form heterodimers, which are incorporated into filaments through a common bipartite polymerizing component, designated as the ZP domain. The latter is composed of two individually folded subdomains, named ZP-N and ZP-C. Here, we have synthesized six 'aggregation-prone' peptides, corresponding to a common interface of human ZP2, ZP3 and ZP4. Experimental results utilizing electron microscopy, X-ray diffraction, ATR FT-IR spectroscopy and polarizing microscopy indicate that these peptides self-assemble forming fibrils with distinct amyloid-like features. Finally, by performing detailed modeling and docking, we attempt to shed some light in the self-assembly mechanism of human ZP proteins.
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